ID EFTU1_YERPP Reviewed; 394 AA.
AC A4TGY7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 10-OCT-2018, entry version 76.
DE RecName: Full=Elongation factor Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=YPDSF_0128;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L.,
RA Schmutz J., Larimer F., Land M., Hauser L., Worsham P., Chu M.,
RA Bearden S., Garcia E., Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
DR EMBL; CP000668; ABP38550.1; -; Genomic_DNA.
DR RefSeq; WP_002212326.1; NZ_CP009715.1.
DR ProteinModelPortal; A4TGY7; -.
DR SMR; A4TGY7; -.
DR EnsemblBacteria; ABP38550; ABP38550; YPDSF_0128.
DR KEGG; ypp:YPDSF_0128; -.
DR PATRIC; fig|386656.14.peg.439; -.
DR HOGENOM; HOG000229290; -.
DR KO; K02358; -.
DR OMA; YGHIDCP; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03697; EFTU_II; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; TF_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1 394 Elongation factor Tu 1.
FT /FTId=PRO_0000337587.
FT DOMAIN 10 204 tr-type G.
FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT REGION 19 26 G1. {ECO:0000250}.
FT REGION 60 64 G2. {ECO:0000250}.
FT REGION 81 84 G3. {ECO:0000250}.
FT REGION 136 139 G4. {ECO:0000250}.
FT REGION 174 176 G5. {ECO:0000250}.
SQ SEQUENCE 394 AA; 43160 MW; 815AC9E6187A5E32 CRC64;
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
ITINTSHVEY DTPARHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFMNKCDM VDDEELLELV EMEVRELLSA YDFPGDDLPV VRGSALKALE
GEAEWEAKII ELAGYLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIVKVG
EEVEIVGIKD TVKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREDIERG QVLAKPGSIK
PHTTFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNINMI
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVIA
//
